Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS
Identifieur interne : 000632 ( PascalFrancis/Corpus ); précédent : 000631; suivant : 000633Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS
Auteurs : YUNFEI LIANG ; YING WAN ; Li-Wen Qiu ; JINGRAN ZHOU ; BING NI ; BO GUO ; QIANG ZOU ; LIYUN ZOU ; WEI ZHOU ; ZHENGCAI JIA ; Xiao-Yan Che ; YUZHANG WUSource :
- Clinical chemistry : (Baltimore, Md.) [ 0009-9147 ] ; 2005.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.
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Format Inist (serveur)
NO : | PASCAL 05-0347652 INIST |
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ET : | Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS |
AU : | YUNFEI LIANG; YING WAN; QIU (Li-Wen); JINGRAN ZHOU; BING NI; BO GUO; QIANG ZOU; LIYUN ZOU; WEI ZHOU; ZHENGCAI JIA; CHE (Xiao-Yan); YUZHANG WU |
AF : | The Institute of Immunology, PLA, The Third Military Medical University/Shapingba District, Chongqing/Chine (1 aut., 2 aut., 4 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 10 aut., 12 aut.); Central Laboratory, Zhujiang Hospital, The Southern Medical University/Guangzhou/Chine (3 aut., 11 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Clinical chemistry : (Baltimore, Md.); ISSN 0009-9147; Coden CLCHAU; Etats-Unis; Da. 2005; Vol. 51; No. 8; Pp. 1382-1396; Bibl. 53 ref. |
LA : | Anglais |
EA : | Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV. |
CC : | 002B24; 002A02 |
FD : | Anticorps; Déterminant antigénique; Cartographie; Nucléocapside; Protéine; Syndrome respiratoire aigu sévère; Coronavirus; Immunité humorale; Biochimie; Biologie clinique; Biologie moléculaire |
FG : | Virose; Infection; Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Poumon pathologie |
ED : | Antibody; Antigenic determinant; Cartography; Nucleocapsid; Protein; Severe acute respiratory syndrome; Coronavirus; Humoral immunity; Biochemistry; Clinical biology; Molecular biology |
EG : | Viral disease; Infection; Coronaviridae; Nidovirales; Virus; Respiratory disease; Lung disease |
SD : | Anticuerpo; Determinante antigénico; Cartografía; Nucleocápside; Proteína; Síndrome respiratorio agudo severo; Coronavirus; Inmunidad humoral; Bioquímica; Biología clínica; Biología molecular |
LO : | INIST-7603.354000138358560100 |
ID : | 05-0347652 |
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<term>Syndrome respiratoire aigu sévère</term>
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<front><div type="abstract" xml:lang="en">Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.</div>
</front>
</TEI>
<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0009-9147</s0>
</fA01>
<fA02 i1="01"><s0>CLCHAU</s0>
</fA02>
<fA03 i2="1"><s0>Clin. chem. : (Baltim. Md.)</s0>
</fA03>
<fA05><s2>51</s2>
</fA05>
<fA06><s2>8</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>YUNFEI LIANG</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>YING WAN</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>QIU (Li-Wen)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>JINGRAN ZHOU</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>BING NI</s1>
</fA11>
<fA11 i1="06" i2="1"><s1>BO GUO</s1>
</fA11>
<fA11 i1="07" i2="1"><s1>QIANG ZOU</s1>
</fA11>
<fA11 i1="08" i2="1"><s1>LIYUN ZOU</s1>
</fA11>
<fA11 i1="09" i2="1"><s1>WEI ZHOU</s1>
</fA11>
<fA11 i1="10" i2="1"><s1>ZHENGCAI JIA</s1>
</fA11>
<fA11 i1="11" i2="1"><s1>CHE (Xiao-Yan)</s1>
</fA11>
<fA11 i1="12" i2="1"><s1>YUZHANG WU</s1>
</fA11>
<fA14 i1="01"><s1>The Institute of Immunology, PLA, The Third Military Medical University</s1>
<s2>Shapingba District, Chongqing</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>12 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Central Laboratory, Zhujiang Hospital, The Southern Medical University</s1>
<s2>Guangzhou</s2>
<s3>CHN</s3>
<sZ>3 aut.</sZ>
<sZ>11 aut.</sZ>
</fA14>
<fA20><s1>1382-1396</s1>
</fA20>
<fA21><s1>2005</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>7603</s2>
<s5>354000138358560100</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2005 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>53 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>05-0347652</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Clinical chemistry : (Baltimore, Md.)</s0>
</fA64>
<fA66 i1="01"><s0>USA</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002B24</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>002A02</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Anticorps</s0>
<s5>02</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Antibody</s0>
<s5>02</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Anticuerpo</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Déterminant antigénique</s0>
<s5>03</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Antigenic determinant</s0>
<s5>03</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Determinante antigénico</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Cartographie</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Cartography</s0>
<s5>05</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Cartografía</s0>
<s5>05</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Nucléocapside</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Nucleocapsid</s0>
<s5>06</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Nucleocápside</s0>
<s5>06</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Protéine</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Protein</s0>
<s5>08</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Proteína</s0>
<s5>08</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0>
<s2>NM</s2>
<s5>09</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0>
<s2>NM</s2>
<s5>09</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0>
<s2>NM</s2>
<s5>09</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>11</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>11</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
<s5>11</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Immunité humorale</s0>
<s5>12</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Humoral immunity</s0>
<s5>12</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Inmunidad humoral</s0>
<s5>12</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Biochimie</s0>
<s5>14</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Biochemistry</s0>
<s5>14</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Bioquímica</s0>
<s5>14</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Biologie clinique</s0>
<s5>15</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Clinical biology</s0>
<s5>15</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Biología clínica</s0>
<s5>15</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Biologie moléculaire</s0>
<s5>17</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Molecular biology</s0>
<s5>17</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Biología molecular</s0>
<s5>17</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Virose</s0>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Viral disease</s0>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Virosis</s0>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Infection</s0>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Infección</s0>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Appareil respiratoire pathologie</s0>
<s5>37</s5>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Respiratory disease</s0>
<s5>37</s5>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0>
<s5>37</s5>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Poumon pathologie</s0>
<s5>38</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0>
<s5>38</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0>
<s5>38</s5>
</fC07>
<fN21><s1>241</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
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<server><NO>PASCAL 05-0347652 INIST</NO>
<ET>Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus : Insight into the humoral immunity of SARS</ET>
<AU>YUNFEI LIANG; YING WAN; QIU (Li-Wen); JINGRAN ZHOU; BING NI; BO GUO; QIANG ZOU; LIYUN ZOU; WEI ZHOU; ZHENGCAI JIA; CHE (Xiao-Yan); YUZHANG WU</AU>
<AF>The Institute of Immunology, PLA, The Third Military Medical University/Shapingba District, Chongqing/Chine (1 aut., 2 aut., 4 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 10 aut., 12 aut.); Central Laboratory, Zhujiang Hospital, The Southern Medical University/Guangzhou/Chine (3 aut., 11 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Clinical chemistry : (Baltimore, Md.); ISSN 0009-9147; Coden CLCHAU; Etats-Unis; Da. 2005; Vol. 51; No. 8; Pp. 1382-1396; Bibl. 53 ref.</SO>
<LA>Anglais</LA>
<EA>Background: The epidemic outbreak of severe acute respiratory syndrome (SARS) posed a worldwide threat to public health and economic stability. Although the pandemic has been contained, concerns over its recurrence remain. It is essential to identify specific diagnostic agents and antiviral vaccine candidates to fight this highly contagious disease. Methods: We generated 14 monoclonal antibodies (mAbs) specific to the SARS coronavirus (SARS-CoV) nucleocapsid (N) protein and used these to thoroughly map the N protein antigenic determinants. We identified the immunodominant antigenic sites responsible for the antibodies in sera from SARS patients and antisera from small animals and differentiated the linear from the conformational antibody-combining sites comprising the natural epitopes by use of yeast surface display. Results: We identified 5 conformational and 3 linear epitopes within the entire N protein; 3 conformational and 3 linear epitopes were immunodominant. The antibody responses to the N protein fragments in mammalian sera revealed that 3 regions of the N protein are strong antigenic domains. We expanded the specificity of the N protein epitope and identified 4 novel conformational epitopes (amino acids 1-69, 68-213, 212-341, and 337-422). Conclusion: The antigenic structures identified for the SARS-CoV N protein, the epitope-specific mAbs, and the serum antibody profile in SARS patients have potential use in the clinical diagnosis and understanding of the protective immunity to SARS-CoV.</EA>
<CC>002B24; 002A02</CC>
<FD>Anticorps; Déterminant antigénique; Cartographie; Nucléocapside; Protéine; Syndrome respiratoire aigu sévère; Coronavirus; Immunité humorale; Biochimie; Biologie clinique; Biologie moléculaire</FD>
<FG>Virose; Infection; Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Poumon pathologie</FG>
<ED>Antibody; Antigenic determinant; Cartography; Nucleocapsid; Protein; Severe acute respiratory syndrome; Coronavirus; Humoral immunity; Biochemistry; Clinical biology; Molecular biology</ED>
<EG>Viral disease; Infection; Coronaviridae; Nidovirales; Virus; Respiratory disease; Lung disease</EG>
<SD>Anticuerpo; Determinante antigénico; Cartografía; Nucleocápside; Proteína; Síndrome respiratorio agudo severo; Coronavirus; Inmunidad humoral; Bioquímica; Biología clínica; Biología molecular</SD>
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